Research Groups
Scientific Coordinator: Ronald Frank (acting)
Chemical Biology investigates the function of biological systems with the means of chemical synthesis. The research of this section focuses on the discovery, synthesis and use of chemical tools that can modulate specifically and selectively the function of target proteins. This work embraces peptides, proteins and low molecular weight drug-like molecules as well as the further development of protein analytics by mass spectroscopy. Biochemical and physical methods aid to investigate interactions of substances with important protein structures. Thereby we support a central goal of the institute which is the elucidation of new principles for pharmacological intervention with biological processes that may ultimately lead to new treatments of diseases.
Chemical Systems Biology (Ronald Frank)
The Chemical Systems Biology Group was newly established in September 2010 and is still in its build-up phase. The group currently works on two research projects: advancement of chemical microarrays and investigation of the cellular protein network regulated by calmodulin.
Chemical Microarray Technology will be established, advanced and
a) used as a tool for the discovery of small molecule ligands of protein targets in the projects of the group, and
b) offered, under the auspices of the Chemical Biology Unit, to other internal and external cooperation partners.
The calmodulinome project, will investigate the growing family of calmodulin (CaM) target proteins, their complex calcium mediated regulation, and their exploration for a systems pharmacological intervention.
Peptide Synthesis (M. Beyermann)
Our group is interested in the molecular basis of interactions between peptide ligands and their membrane-embedded receptors, in particular G protein-coupled receptors class B. We investigate ligand-binding activities of extracellular domains (EC1-4) of CRF receptors and look at the contribution of these domains to the receptor-affinity of ligands.
Peptide Lipid Interaction / Peptide Transport (M. Dathe/J. Oehlke)
The group is interested in the structural requirements of peptides as uptake-promoting and targeting tools for attached cargos and lipid-based carriers. Furthermore, we look at the role of the lipid matrix in mediating transmembrane transport and in modulating the activity and selectivity of antimicrobial peptides.
Mass Spectrometry (E. Krause)
Mass spectrometry is a key technology in proteome research. Our research group focuses on the elucidation of functionally important proteins and their post-translational modifications using electrospray ionisation (ESI) and matrix-assisted laser desorption/ionisation (MALDI) mass spectrometry in combination with miniaturized separation techniques and stable isotope labelling. These methods have allowed us to study protein-protein interactions which play important roles in processes such as T-cell signalling and the assembly of spliceosomes.
Protein Chemistry (D. Schwarzer)
Our group is developing chemical tools to study the physiological function of posttranslational protein modifications. A central goal is the development of probes that serve as baits to trap, isolate and identify modification-specific binding proteins.
Please note
Prof. Dirk Schwarzer has accepted the chair for Biochemistry at theEberhard Karls Universität Tübingen in Octobre 2011, but he still has coworkers at the FMP.
Medicinal Chemistry (J. Rademann)
We develop strategies in the areas of synthetic organic chemistry, library design, and bioassays. Most protein targets of the group are disease-related enzymes including proteases and phosphatases relevant to clinical indications including cancer, Alzheimer, tuberculosis, and SARS. Recently, the targeted proteins have been extended towards receptors and protein-protein interactions.
Please note
Prof. Jörg Rademann has accepted the chair for Medicinal Chemistry at theUniversität Leipzig in April 2010, but he still has coworkers at the FMP.
Biophysics of Membrane Proteins (S. Keller)
We are interested in the mechanisms of folding and reconstitution of polytopic a-helical membrane proteins (such as receptors and channels) as well as of protein–protein and protein–ligand interactions. We use a range of biophysical methods (in particular, spectroscopy and calorimetry) to examine the thermodynamics and kinetics of this pharmacologically relevant class of proteins and their interactions with small molecules.
Please note that Sandro Keller was appointed Junior Professor for Biophysics at the
Technische Universität Kaiserlautern in November 2009. He still has coworkers at the FMP.
